GenomeNet

Database: UniProt
Entry: A2WDL6_9BURK
LinkDB: A2WDL6_9BURK
Original site: A2WDL6_9BURK 
ID   A2WDL6_9BURK            Unreviewed;       646 AA.
AC   A2WDL6;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Hemolysin {ECO:0000313|EMBL:EAY70062.1};
GN   ORFNames=BDAG_02841 {ECO:0000313|EMBL:EAY70062.1};
OS   Burkholderia dolosa AU0158.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY70062.1, ECO:0000313|Proteomes:UP000053482};
RN   [1] {ECO:0000313|Proteomes:UP000053482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA   DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA   Alvarado L., Lory S., LiPuma J.;
RT   "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CH482381; EAY70062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2WDL6; -.
DR   HOGENOM; CLU_423718_0_0_4; -.
DR   Proteomes; UP000053482; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002550; CNNM.
DR   InterPro; IPR044751; Ion_transp-like_CBS.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   PANTHER; PTHR43099:SF5; INTEGRAL MEMBRANE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43099; UPF0053 PROTEIN YRKA; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01595; CNNM; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS51846; CNNM; 1.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000053482};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU01193};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}.
FT   TRANSMEM        87..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..191
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000259|PROSITE:PS51846"
FT   DOMAIN          218..278
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          284..341
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          416..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  70258 MW;  085F61E83B3FC3A9 CRC64;
     MALNGFFVAA EFGLVKLRTT RVKTLARKHG LRGRILGVVH GRLDAYLSAC QLGITLASLG
     LGWIGEPAFA ELIGPLLDLL GVESERVVHL ISLVFAFSLI SFLHIVVGEL APKSMAIRQP
     EKVGLWVALP LYAFYWAMYP AIWLLNTSAN AVLRLAGLSA DHGSDAHYST DELKLILRSR
     RSTAGGAAQP TRGSYSNDEW NTLAHSLDFS SMTVSDLMRP AHEMIGLRRD LPLPDNMEIV
     ARHRFSRYPL FADASRERVF GLIHLKDLLL ARHAGAALDD LSDYVRPVQY VKPDMPALDL
     FRRFRKGAPH FALVGNKREK PIGFLTLDNL LGALVGQIHD EFHQGDADWS RLDDGTLMGK
     GSLPVVSLEQ ALGIDIDEGR AESRRRAGDP GAERSAVRRA ARVVRSLRRR REEDEWASDR
     ARARLSEDDE GKPTNDGLVT ARAMNATLPR CCVITPEPAS ASAADCRAFV DRLEAVLARG
     DTLVQLRAKS LDAAAFARLA ADALARCDAA GAQLMLNGPI DAAGVMRLDG AGWHLDGAAL
     RTVAQRPLPA DTPVSAACHT ADDLLLAARA GADFVTLSPV RPTLSHPGAP TLGWEKFDAL
     GRAGRDARLR ARRDDARASR RRASASRIRN RGYSRVLVSR GAAARG
//
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